+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Nucleoside diphosphate kinase and GTP-binding proteins. Possible mechanisms of coupling



Nucleoside diphosphate kinase and GTP-binding proteins. Possible mechanisms of coupling



Biofizika 53(6): 922-928



The results of numerous investigations during the last 20 years have shown that nucleoside diphosphate kinase (NDP kinase) is a multifunctional protein. In this paper, the current data are analyzed indicating that one of the possible mechanisms by which NDP kinase manifests its multifunctional role is its participation in the activation (or regulation) of heterotrimeric GTP-binding proteins (G proteins). We demonstrate that one of the NDP kinase isoforms dynamically interacts with the retinal rod G protein transducin (Gt) and phosphorylates its beta-subunit at histidine residue (His 266). It is also shown that it leads to the consecutive transfer of the phosphate group to the GDP in the active center of G protein alpha-subunit and G protein activation. The advantages of this mechanism are considered as compared to the classic G protein activation mechanism, GDP/GTP exchange.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 054683915

Download citation: RISBibTeXText

PMID: 19137672


Related references

Microtubules and nucleoside diphosphate kinase nucleoside diphosphate kinase binds to co purifying contaminants rather than microtubule proteins. Biochemical Journal 232(3): 651-656, 1985

Conversion of GDP into GTP by nucleoside diphosphate kinase on the GTP-binding proteins. Journal of Biological Chemistry 265(35): 21536-21540, 1990

Physiological correlation between nucleoside-diphosphate kinase and the enzyme-associated guanine nucleotide binding proteins. Biochemical and Biophysical Research Communications 143(2): 552-559, 1987

Regulatory GTP-binding proteins (ADP-ribosylation factor, Gt, and RAS) are not activated directly by nucleoside diphosphate kinase. Journal of Biological Chemistry 267(25): 18182, 1992

Direct activation of guanine nucleotide binding proteins through a high-energy phosphate-transfer by nucleoside diphosphate-kinase. Biochemical and Biophysical Research Communications 148(1): 300-307, 1987

Adenosine 5'-diphosphate binding and the active site of nucleoside diphosphate kinase. Biochemistry 33(2): 459-467, 1994

X-ray analysis of azido-thymidine diphosphate binding to nucleoside diphosphate kinase. Proceedings of the National Academy of Sciences of the United States of America 94(14): 7162-7165, 1997

Quantification of uridine 5'-diphosphate (UDP)-glucose by high-performance liquid chromatography and its application to a nonradioactive assay for nucleoside diphosphate kinase using UDP-glucose pyrophosphorylase as a coupling enzyme. Analytical Biochemistry 323(2): 188-196, 2003

The nucleoside diphosphate kinase of Mycobacterium smegmatis: Identification of proteins that modulate specificity of nucleoside triphosphate synthesis by the enzyme. Molecular Microbiology 24(3): 477-487, 1997

Nucleoside diphosphate kinase of Mycobacterium smegmatis Identification of proteins that modulate specificity of nucleoside triphosphate synthesis by the enzyme. Abstracts of the General Meeting of the American Society for Microbiology 97: 567, 1997

Identification of a phosphate-incorporating protein from bovine liver as nucleoside diphosphate kinase and isolation of 1-32P-phosphohistidine, 3-32P-phosphohistidine, and N-epsilon-32P-phospholysine from erythrocytic nucleoside diphosphate kinase, incubated with adenosine triphosphate-32P. Journal of Biological Chemistry 243(14): 3947-3952, 1968

Coupling between catalysis and oligomeric structure in nucleoside diphosphate kinase. Journal of Biological Chemistry 273(8): 4436-4442, 1998